Recruitment of coat-protein-complex proteins on to phagosomal membranes is regulated by a brefeldin A-sensitive ADP-ribosylation factor

Author:

BERÓN Walter1,MAYORGA Luis S.1,COLOMBO Maria I.1,STAHL Philip D.2

Affiliation:

1. Instituto de Histología y Embriología-CONICET, Universidad Nacional de Cuyo, Casilla de Correo 56, (5500) Mendoza, Argentina

2. Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, Missouri 63110, U.S.A.

Abstract

Particle internalization in macrophages is followed by a complex maturation process. We have previously observed that proteins bound to phagocytosed particles are sorted from phagosomes into a heterogeneous population of vesicles that fuse with endosomes. However, the mechanism and the protein machinery involved in the formation of these phagosome-derived vesicles are largely unknown. It has been shown that vesicles coated with coat protein complex type I (COPI) have a role in both secretion and endocytosis. To address the possibility that COPI proteins might participate in the formation of phagosome-derived vesicles we studied the recruitment of β-COP to highly purified phagosomes. The binding of β-COP to phagosomal membranes was regulated by nucleotides and inhibited by brefeldin A (BFA). An ADP-ribosylation factor 1 (ARF1) mutant defective in GTP hydrolysis supported the binding of β-COP to phagosomes independently of added nucleotide. AlF4 and Gβγ subunits, agents known to modulate heterotrimeric G-protein activity, were tested in the β-COP binding assay. AlF4 increased β-COP association, whereas binding was inhibited by the addition of Gβγ subunits. Our results suggest that COP proteins are recruited to phagosomal membranes by a mechanism that involves heterotrimeric GTP-binding proteins and a BFA-sensitive ARF. In addition, our findings indicate that COPI proteins are involved in the recycling of components from phagosomes to the cell surface.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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